MolNFT v1 · #85072 · protein

Structure of the global transcription regulator fapr from staphylococcus aureus

4A0Y · Transcription factor fapr: “Structure of the global transcription regulator fapr from staphylococcus aureus”. X-ray diffraction, 1 ligand (CL), 5 pockets (best druggability 0.62). MolNFT v1 #85072 on GenesisL1: 3D structure, binding…

PDB: 4A0Y
Type: protein
Length: 302 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription factor fapr
UniProt: D6UB50
Ligands: CL
Pockets: 5 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription factor fapr	protein	184	38% helix, 34% strand	D6UB50
B	Transcription factor fapr	protein	118	18% helix, 53% strand	D6UB50

Ligands and binding sites

CL · Chloride ion · ion · 9 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.62	0.92	23	CL
2	53	0.57	0.90	17	empty
3	73	0.35	0.76	18	empty
4	89	0.33	0.73	14	empty
5	55	0.32	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 1365 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

4A0Y · Structure of the global transcription regulator FapR from Staphylococcus aureus · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt D6UB50
Elsewhere: RCSB PDB 4A0Y · PDBe 4A0Y · UniProt D6UB50

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